Structural Phosphoproteins Associated with Measles Virus Nucleocapsids from Persistently Infected Cells

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Abstract
Summary Measles virus nucleocapsids were labelled with 3H-amino acids and 32P-orthophosphate, and purified from the cytoplasm of persistently infected human amnion cells (AV+). When analysed by SDS-PAGE, the two major capsid-associated polypeptides (P, mol. wt. 69000, and NP, mol. wt. 60000) were shown to be phosphorylated. Subsequent characterization of the phosphorylated polypeptides by acid hydrolysis and high voltage paper electrophoresis showed that serine and threonine were the major phosphorylated amino acid species. The similarities between the peptide phosphorylation patterns obtained in these studies and those reported earlier for the virus phosphoproteins produced in acute infections (Robbins & Bussell, 1979) indicate that major phosphorylative modifications of the capsid proteins are not involved in measles virus persistence in AV3 cells.

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